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O28440

- ASPD_ARCFU

UniProt

O28440 - ASPD_ARCFU

Protein

Probable L-aspartate dehydrogenase

Gene

nadX

Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    • Comment

    Functioni

    Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate.UniRule annotation

    Catalytic activityi

    L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111NAD; via amide nitrogenUniRule annotation
    Binding sitei162 – 1621NADUniRule annotation
    Active sitei189 – 1891UniRule annotation

    GO - Molecular functioni

    1. aspartate dehydrogenase activity Source: UniProtKB-EC
    2. NAD binding Source: UniProtKB-HAMAP
    3. NADP binding Source: UniProtKB-HAMAP
    4. oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Source: UniProtKB-HAMAP

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB-HAMAP
    2. NADP catabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    BioCyciAFUL224325:GJBC-1873-MONOMER.
    SABIO-RKO28440.
    UniPathwayiUPA00253; UER00456.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable L-aspartate dehydrogenaseUniRule annotation (EC:1.4.1.21UniRule annotation)
    Gene namesi
    Name:nadXUniRule annotation
    Ordered Locus Names:AF_1838
    OrganismiArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
    Taxonomic identifieri224325 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeArchaeoglobus
    ProteomesiUP000002199: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Probable L-aspartate dehydrogenasePRO_0000144894Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi224325.AF1838.

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Helixi10 – 2112
    Beta strandi25 – 306
    Beta strandi39 – 424
    Helixi43 – 464
    Beta strandi52 – 565
    Helixi60 – 7213
    Beta strandi76 – 805
    Helixi82 – 865
    Helixi88 – 10114
    Beta strandi105 – 1073
    Helixi115 – 1206
    Helixi122 – 1243
    Beta strandi125 – 13511
    Helixi136 – 1383
    Beta strandi143 – 1497
    Helixi150 – 1567
    Helixi162 – 17110
    Beta strandi176 – 1838
    Beta strandi185 – 19511
    Beta strandi198 – 2069
    Beta strandi212 – 2165
    Helixi217 – 23115
    Beta strandi232 – 2354

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DC1X-ray1.90A/B1-236[»]
    ProteinModelPortaliO28440.
    SMRiO28440. Positions 1-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO28440.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the L-aspartate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1712.
    KOiK06989.
    OMAiECAGHSA.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_01265. NadX.
    InterProiIPR005106. Asp/hSer_DH_NAD-bd.
    IPR002811. Asp_DH.
    IPR022487. Asp_DH_arc.
    IPR020626. Asp_DH_prok.
    IPR011182. L-Asp_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01958. DUF108. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.
    TIGRFAMsiTIGR03855. NAD_NadX. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O28440-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLVGLIGYGA IGKFLAEWLE RNGFEIAAIL DVRGEHEKMV RGIDEFLQRE    50
    MDVAVEAASQ QAVKDYAEKI LKAGIDLIVL STGAFADRDF LSRVREVCRK 100
    TGRRVYIASG AIGGLDAIFS ASELIEEIVL TTRKNWRQFG RKGVIFEGSA 150
    SEAAQKFPKN LNVAATLSIA SGKDVKVRLV ADEVEENIHE ILVRGEFGEM 200
    EIRVRNRPMR ENPKTSYLAA LSVTRILRNL KEGLVV 236
    Length:236
    Mass (Da):26,208
    Last modified:January 1, 1998 - v1
    Checksum:i29218ACC7F919F52
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89415.1.
    PIRiE69479.
    RefSeqiNP_070664.1. NC_000917.1.

    Genome annotation databases

    EnsemblBacteriaiAAB89415; AAB89415; AF_1838.
    GeneIDi1485059.
    KEGGiafu:AF1838.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000782 Genomic DNA. Translation: AAB89415.1 .
    PIRi E69479.
    RefSeqi NP_070664.1. NC_000917.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DC1 X-ray 1.90 A/B 1-236 [» ]
    ProteinModelPortali O28440.
    SMRi O28440. Positions 1-236.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224325.AF1838.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB89415 ; AAB89415 ; AF_1838 .
    GeneIDi 1485059.
    KEGGi afu:AF1838.

    Phylogenomic databases

    eggNOGi COG1712.
    KOi K06989.
    OMAi ECAGHSA.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00456 .
    BioCyci AFUL224325:GJBC-1873-MONOMER.
    SABIO-RK O28440.

    Miscellaneous databases

    EvolutionaryTracei O28440.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    HAMAPi MF_01265. NadX.
    InterProi IPR005106. Asp/hSer_DH_NAD-bd.
    IPR002811. Asp_DH.
    IPR022487. Asp_DH_arc.
    IPR020626. Asp_DH_prok.
    IPR011182. L-Asp_DH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF01958. DUF108. 1 hit.
    PF03447. NAD_binding_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
    TIGRFAMsi TIGR03855. NAD_NadX. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus."
      Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G.
      , Gill S.R., Kirkness E.F., Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
      Nature 390:364-370(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.

    Entry informationi

    Entry nameiASPD_ARCFU
    AccessioniPrimary (citable) accession number: O28440
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia.UniRule annotation

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3